Solution structure of antifreeze glycopeptides. Determination of the major conformers of the glycosidic linkages

S. W. Homans; A. L. DeVries; S. B. Parker

doi:10.1016/0014-5793(85)80970-4

Solution structure of antifreeze glycopeptides. Determination of the major conformers of the glycosidic linkages

S. W. Homans, A. L. DeVries, S. B. Parker

Evolution, Ecology, and Behavior

Research output: Contribution to journal › Article › peer-review

Abstract

Using data obtained from ¹H-¹H correlated spectroscopy and one- and two-dimensional NOE measurements, we have determined the preferential solution conformation of the disaccharide unit Galβ(1-3)Gal-NAc in the antifreeze glycopeptide (Galß(l-3)GalNAcαl-Thr-Ala-Ala)_n derived from the blood of the antarctic fish Trematomas borchgrevinki. The disaccharide, which is a rigid unit, exists with a restricted orientation about the GalNAc-αl-Thr linkage. Preliminary evidence indicates that the backbone (Ala-Ala-Thr)_n lies in an extended helical conformation. Antifreeze glycopeptide¹H NMR Glycosidic linkage Dissaccharide structure Nuclear Overhauser effect.

Original language	English (US)
Pages (from-to)	133-137
Number of pages	5
Journal	FEBS Letters
Volume	183
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(85)80970-4
State	Published - Apr 8 1985

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(85)80970-4

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title = "Solution structure of antifreeze glycopeptides. Determination of the major conformers of the glycosidic linkages",

abstract = "Using data obtained from 1H-1H correlated spectroscopy and one- and two-dimensional NOE measurements, we have determined the preferential solution conformation of the disaccharide unit Galβ(1-3)Gal-NAc in the antifreeze glycopeptide (Gal{\ss}(l-3)GalNAcαl-Thr-Ala-Ala)n derived from the blood of the antarctic fish Trematomas borchgrevinki. The disaccharide, which is a rigid unit, exists with a restricted orientation about the GalNAc-αl-Thr linkage. Preliminary evidence indicates that the backbone (Ala-Ala-Thr)n lies in an extended helical conformation. Antifreeze glycopeptide 1H NMR Glycosidic linkage Dissaccharide structure Nuclear Overhauser effect.",

author = "Homans, {S. W.} and DeVries, {A. L.} and Parker, {S. B.}",

note = "Funding Information: The authors wish to thank Drs R.A. Dwek, T.W. Rademachear nd Professor R.J.P. Williams for encouragementa nd support. S.W.H. is a membero f the Oxford Enzyme Group. This work was supportedi n part by a grant from Monsanto Co., USA.",

year = "1985",

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doi = "10.1016/0014-5793(85)80970-4",

language = "English (US)",

volume = "183",

pages = "133--137",

journal = "FEBS Letters",

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T1 - Solution structure of antifreeze glycopeptides. Determination of the major conformers of the glycosidic linkages

AU - Homans, S. W.

AU - DeVries, A. L.

AU - Parker, S. B.

N1 - Funding Information: The authors wish to thank Drs R.A. Dwek, T.W. Rademachear nd Professor R.J.P. Williams for encouragementa nd support. S.W.H. is a membero f the Oxford Enzyme Group. This work was supportedi n part by a grant from Monsanto Co., USA.

PY - 1985/4/8

Y1 - 1985/4/8

N2 - Using data obtained from 1H-1H correlated spectroscopy and one- and two-dimensional NOE measurements, we have determined the preferential solution conformation of the disaccharide unit Galβ(1-3)Gal-NAc in the antifreeze glycopeptide (Galß(l-3)GalNAcαl-Thr-Ala-Ala)n derived from the blood of the antarctic fish Trematomas borchgrevinki. The disaccharide, which is a rigid unit, exists with a restricted orientation about the GalNAc-αl-Thr linkage. Preliminary evidence indicates that the backbone (Ala-Ala-Thr)n lies in an extended helical conformation. Antifreeze glycopeptide 1H NMR Glycosidic linkage Dissaccharide structure Nuclear Overhauser effect.

AB - Using data obtained from 1H-1H correlated spectroscopy and one- and two-dimensional NOE measurements, we have determined the preferential solution conformation of the disaccharide unit Galβ(1-3)Gal-NAc in the antifreeze glycopeptide (Galß(l-3)GalNAcαl-Thr-Ala-Ala)n derived from the blood of the antarctic fish Trematomas borchgrevinki. The disaccharide, which is a rigid unit, exists with a restricted orientation about the GalNAc-αl-Thr linkage. Preliminary evidence indicates that the backbone (Ala-Ala-Thr)n lies in an extended helical conformation. Antifreeze glycopeptide 1H NMR Glycosidic linkage Dissaccharide structure Nuclear Overhauser effect.

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JO - FEBS Letters

JF - FEBS Letters

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Solution structure of antifreeze glycopeptides. Determination of the major conformers of the glycosidic linkages

Abstract

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